Ricin

Ribosome-inactivating protein (Ricin A chain)
Ribosome-inactivating protein (Ricin A chain)
Identifiers
Symbol	RIP
Pfam	PF00161
InterPro	IPR001574
PROSITE	PDOC00248
SCOP2	1paf / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search for
Structures	Swiss-model
Domains	InterPro

Ricin
Ricin
	Ricin structure (PDB: 2AAI). The A chain is shown in blue and the B chain in orange.
Identifiers
Organism	Ricinus communis
Symbol	RCOM_2159910
Entrez	8287993
RefSeq (mRNA)	XM_002534603.1
RefSeq (Prot)	XP_002534649.1
UniProt	P02879
Other data
EC number	3.2.2.22
Chromosome	whole genome: 0 - 0.01 Mb
Structures
Search for
Structures	Swiss-model
Domains	InterPro

Ricin-type beta-trefoil lectin domain (Ricin B chain)

Identifiers

Symbol

N/A

Pfam clan

1abr / SCOPe / SUPFAM

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Ricin (/ˈraɪsɪn/ RY-sin) is a lectin (a carbohydrate-binding protein) and a highly potent toxin produced in the seeds of the castor oil plant, Ricinus communis. The median lethal dose (LD₅₀) of ricin for mice is around 22 micrograms per kilogram of body weight via intraperitoneal injection. Oral exposure to ricin is far less toxic. An estimated lethal oral dose in humans is approximately one milligram per kilogram of body weight.^[1]

Ricin is a toxalbumin and was first described by Peter Hermann Stillmark, the founder of lectinology. Ricin is chemically similar to robin.

^ "Ricin (from Ricinus communis) as undesirable substances in animal feed-Scientific Opinion of the Panel on Contaminants in the Food Chain". EFSA Journal. 6 (9). European Food Safety Authority: 726. September 2008. doi:10.2903/j.efsa.2008.726.

[Efsa.europa.eu-1] "Ricin (from Ricinus communis) as undesirable substances in animal feed-Scientific Opinion of the Panel on Contaminants in the Food Chain". EFSA Journal. 6 (9). European Food Safety Authority: 726. September 2008. doi:10.2903/j.efsa.2008.726.

[1]